Adsorption of BSA and hemoglobin on hydroxyapatite support: Equilibria and multicomponent dynamic adsorption

被引:32
|
作者
Fargues, C [1 ]
Bailly, M [1 ]
Grevillot, G [1 ]
机构
[1] Ecole Natl Super Ind Chim, CNRS, Lab Sci Genie Chim, F-54001 Nancy, France
关键词
chromatography; multicomponent; intraparticle diffusion; experimental data; proteins;
D O I
10.1023/A:1008822918494
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Interactions of Bovin Serum Albumin and Hemoglobin with an hydroxyapatite gel (HA-Ultrogel, Sepracor), have been studied separately in batch experiments. The adsorption isotherms are of the Langmuir type and can be used directly to scale column operations. For adsorption of hemoglobin alone, in column at pH 6.8 (equal to its isoelectric point) we notice that a classical intraparticle transfer model, based on a constant effective diffusion coefficient represents perfectly the symmetrical breakthrough curve. For acid pH values (pH 5.8), Langmuir isotherms of BSA and hemoglobin adsorptions showed a strong curvature, sign of a quite irreversible adsorption and breakthrough curves obtained under these conditions, exhibit a high dissymmetrical shape for both proteins. In that case, a model of diffusion based on the adsorption on two types of independent sites, with two intraparticle transfer coefficients, gives a good representation of the breakthrough for adsorption of both proteins separately. Binary mixtures of these components were prepared and injected in columns packed with the same support. Competitive Langmuir equation, based on the results obtained in monocomponent batch experiments, give a very good fit to our system. The intraparticle transfer in that case seems to be facilitated, and one effective coefficient alone is enough to predict the breakthrough curves obtained. This behaviour may be the result of an increase of the solution ionic strength, and of the smaller irreversibility feature of the adsorption when proteins are in competition.
引用
收藏
页码:5 / 16
页数:12
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